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1knx
From Proteopedia
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| - | [[Image:1knx.gif|left|200px]] | + | [[Image:1knx.gif|left|200px]] |
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| - | '''HPr kinase/phosphatase from Mycoplasma pneumoniae''' | + | {{Structure |
| + | |PDB= 1knx |SIZE=350|CAPTION= <scene name='initialview01'>1knx</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HPr kinase/phosphatase from Mycoplasma pneumoniae''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KNX is a [ | + | 1KNX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_pneumoniae Mycoplasma pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNX OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae., Allen GS, Steinhauer K, Hillen W, Stulke J, Brennan RG, J Mol Biol. 2003 Feb 28;326(4):1203-17. PMID:[http:// | + | Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae., Allen GS, Steinhauer K, Hillen W, Stulke J, Brennan RG, J Mol Biol. 2003 Feb 28;326(4):1203-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12589763 12589763] |
[[Category: Mycoplasma pneumoniae]] | [[Category: Mycoplasma pneumoniae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: walker a box]] | [[Category: walker a box]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:55 2008'' |
Revision as of 10:19, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HPr kinase/phosphatase from Mycoplasma pneumoniae
Overview
HPr kinase/phosphatase (HPrK/P) modifies serine 46 of histidine-containing protein (HPr), the phosphorylation state of which is the control point of carbon catabolite repression in low G+C Gram-positive bacteria. To understand the structural mechanism by which HPrK/P carries out its dual, competing activities we determined the structure of full length HPrK/P from Mycoplasma pneumoniae (PD8 ID, 1KNX) to 2.5A resolution. The enzyme forms a homo-hexamer with each subunit containing two domains connected by a short loop. The C-terminal domain contains the well-described P-loop (Walker A box) ATP binding motif and takes a fold similar to phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as recently described in other HPrK/P structures. As expected, the C-terminal domain is very similar to the C-terminal fragment of Lactobacillus casei HPrK/P and the C-terminal domain of Staphylococcus xylosus HPrK/P; the N-terminal domain is very similar to the N-terminal domain of S.xylosus HPrK/P. Unexpectedly, the N-terminal domain resembles UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase (MurE), yet the function of this domain is unclear. We discuss these observations as well as the structural significance of mutations in the P-loop and HPrK/P family sequence motif.
About this Structure
1KNX is a Single protein structure of sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA.
Reference
Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae., Allen GS, Steinhauer K, Hillen W, Stulke J, Brennan RG, J Mol Biol. 2003 Feb 28;326(4):1203-17. PMID:12589763
Page seeded by OCA on Thu Mar 20 12:19:55 2008
